Registro:

Referencias:

• Abbott, W.M., Feizi, T., Soluble 14-kDa beta-galactoside-specific bovine lectin Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain (1991) J Biol Chem., 266, pp. 5552-5557
• Anisimov, V.N., Cavasotto, C.N., Quantum mechanical binding free energy calculation for phosphopeptide inhibitors of the Lck SH2 domain (2011) J Comput Chem., 32, pp. 2254-2263
• Ashraf, G.M., Banu, N., Ahmad, A., Singh, L.P., Kumar, R., Purification, characterization, sequencing and biological chemistry of galectin-1 purified from Capra hircus (goat) heart (2011) Protein J., 30, pp. 39-51
• Baker, L.M., Poole, L.B., Catalytic mechanism of thiol peroxidase from Escherichia coli Sulfenic acid formation and overoxidation of essential CYS61 (2003) J Biol Chem., 278, pp. 9203-9211
• Bas, D.C., Rogers, D.M., Jensen, J.H., Very fast prediction and rationalization of pKa values for protein-ligand complexes (2008) Proteins., 73, pp. 765-783
• Bashford, D., Case, D.A., Generalized born models of macro-molecular solvation effects (2000) Annu Rev Phys Chem., 51, pp. 129-152
• Berendsen, H.J.C., Postma, J.P.M., Van Gunsteren, W.F., DiNola, A., Haak, J.R., Molecular-dynamics with coupling to an external bath (1984) J Chem Phys., 81, pp. 3684-3690
• Blidner, A.G., Rabinovich, G.A., Sweetening' pregnancy: Galectins at the fetomaternal interface (2013) Am J Reprod Immunol., 69, pp. 369-382
• Brigelius-Flohé, R., Flohé, L., Basic principles and emerging concepts in the redox control of transcription factors (2011) Antioxid Redox Sign., 15, pp. 2335-2381
• Carballal, S., Radi, R., Kirk, M.C., Barnes, S., Freeman, B.A., Alvarez, B., Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite (2003) Biochemistry., 42, pp. 9906-9914
• Case, D.A., Darden, T.A., Cheatham III, T.E., Simmerling, C.L., Wang, J., Duke, R.E., Luo, R., Crowley, M., (2006) AMBER 9. San Francisco, , CA: University of California
• Cho, M., Cummings, R.D., Characterization of monomeric forms of galectin-1 generated by site-directed mutagenesis (1996) Biochemistry., 35, pp. 13081-13088
• Clackson, T., Detlef, G., Jones, P.T., (1991) General application of PCR to gene cloning and manipulation, , In: McPherson M.J., Quirke P., Taylor G.R., editors. PCR, a practical approach. Oxford: IRL Press at Oxford University Press
• Cooper, D.N.W., Galectinomics: Finding themes in complexity (2002) Biochim Biophys Acta., 1572, pp. 209-231
• Dam, T.K., Brewer, C.F., Maintenance of cell surface glycan density by lectin-glycan interactions: A homeostatic and innate immune regulatory mechanism (2010) Glycobiology., 20, pp. 1061-1064
• Delaunay, A., Pflieger, D., Barrault, M.B., Vinh, J., Toledano, M.B., A thiol peroxidase is an H2O2 receptor and redox-Transducer in gene activation (2002) Cell., 111, pp. 471-481
• Ferrer-Sueta, G., Manta, B., Botti, H., Radi, R., Trujillo, M., Denicola, A., Factors affecting protein thiol reactivity and specificity in peroxide reduction (2011) Chem Res Toxicol., 24, pp. 434-450
• Flohé, L., Toppo, S., Cozza, G., Ursini, F., A comparison of thiol peroxidase mechanisms (2011) Antioxid Redox Sign., 15, pp. 763-780
• Flohé, L., Ursini, F., Peroxidase: A term of many meanings (2008) Antioxid Redox Sign., 10, pp. 1485-1490
• Georgiou, G., Masip, L., Biochemistry An overoxidation journey with a return ticket (2003) Science., 300, pp. 592-594
• Goldman, R., Stoyanovsky, D.A., Day, B.W., Kagan, V.E., Reduction of phenoxyl radicals by thioredoxin results in selective oxidation of its SH-groups to disulfides An antioxidant function of thioredoxin (1995) Biochemistry., 34, pp. 4765-4772
• Guardia, C.M.A., Gauto, D.F., Di Lella, S., Rabinovich, G.A., Marti, M.A., Estrin, D.A., An integrated computational analysis of the structure, dynamics and ligand binding interactions of the human galectin network (2011) J Chem Inf Model., 51, pp. 1918-1930
• Hirabayashi, J., Kasai, K., Effect of amino acid substitution by siteddirected mutagenesis on the carbohydrate recognition and stability of human 14-kDa beta-galactoside-binding lectin (1991) J Biol Chem., 266, pp. 23648-23653
• Hirabayashi, J., Kawasaki, H., Suzuki, K., Kasai, K., Complete amino acid sequence of 14 kDa beta-galactoside-binding lectin of chick embryo (1987) J Biochem (Tokyo)., 101, pp. 987-995
• Hornak, V., Aberl, R., Okur, A., Strockbine, B., Roitberg, A.E., Simmerling, C., Comparison of multiple Amber force fields and development of improved protein backbone parameters (2006) Proteins., 65, pp. 712-725
• Hou, T., Wang, J., Li, Y., Wang, W., Assessing the performance of the MM/ PBSA and MM/GBSA methods: I. The accuracy of binding free energy calculations based on molecular dynamics simulations (2011) J Chem Inf Model., 51, pp. 69-82
• Humphrey, W., Dalke, A., Schulten, K., VMD-visual molecular dynamics (1996) J Molec Graphics., 14, pp. 33-38
• Ilarregui, J.M., Croci, D.O., Bianco, G.A., Toscano, M., Salatino, M., Vermeuen, M.E., Geffner, J.R., Rabinovich, G.A., Tolerogenic signals delivered by dendritic cells to T cells through a galectin-1-driven immunoregulatory circuit involving interleukin 27 and interleukin 10 (2009) Nat Immunol., 10, pp. 981-991
• Inagaki, Y., Sohma, Y., Horie, H., Nozawa, R., Kadoya, T., Oxidized galectin-1 promotes axonal regeneration in peripheral nerves but does not possess lectin properties (2000) Eur J Biochem., 267, pp. 2955-2964
• Jorgensen, W.L., Chandrasekhar, J., Madura, J.D., Impey, R.W., Klein, M.L., Comparison of simple potential functions for simulating liquid water (1983) J Chem Phys., 79, pp. 926-935
• Kadoya, T., Horie, H., Structural and functional studies of galectin-1: A novel axonal regeneration-promoting activity for oxidized galectin-1 (2005) Curr Drug Targets., 6, pp. 375-383
• Kirschner, K.N., Yongye, A.B., Tschampel, S.M., González-Outeiriño, J., Daniels, C.R., Foley, B.L., Woods, R.J., GLYCAM06: A generalizable biomolecular force field. Carbohydrates (2008) J Comput Chem., 29, pp. 622-655
• Knapp, B., Lederer, N., Omasits, U., Schreiner, W., VmdICE: A plug-in for rapid evaluation of molecular dynamics simulations using VMD (2010) J Comput Chem., 31, pp. 2868-2873
• Kongsted, J., Söderhjelm, P., Ryde, U., How accurate are continuum solvation models for drug-like molecules? (2009) J Comput Aided Mol Des., 23, pp. 395-409
• Lange, F., Brandt, B., Tiedge, M., Jonas, L., Jeschke, U., Pöhland, R., Walzel, H., Galectin-1 induced activation of the mitochondrial apoptotic pathway: Evidence for a connection between death-receptor and mitochondrial pathways in human Jurkat T lymphocytes (2009) Histochem Cell Biol., 132, pp. 211-223
• Lopez-Lucendo, M.F., Solis, D., Andre, S., Hirabayashi, J., Kasai, K., Kaltner, H., Gabius, H.J., Romero, A., Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by singlesite mutations and their impact on the thermodynamics of ligand binding (2004) J Mol Biol., 343, pp. 957-970
• Nishi, N., Abe, A., Iwaki, J., Yoshida, H., Itoh, A., Shoji, H., Kamitori, S., Nakamura, T., Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1 (2008) Glycobiology., 18, pp. 1065-1073
• Oda, Y., Kasai, K., Purification and characterization of beta-galactoside-binding lectin from chick embryonic skin (1983) Biochim Biophys Acta., 761, pp. 237-245
• Pace, K.E., Hahn, H.P., Baum, L.G., Preparation of recombinant human galectin-1 and use in T-cell death assays (2003) Methods Enzymol., 363, pp. 499-518
• Pande, A.H., Gupta Sumati, R.K., Hajela, K., Oxidation of goat hepatic galectin-1 induces change in secondary structure (2003) Protein Pept Lett., 10, pp. 265-275
• Pascual, M.B., Mata-Cabana, A., Florencio, F.J., Lindahl, M., Cejudo, F.J., Overoxidation of 2-Cys peroxiredoxin in prokaryotes: Cyanobacterial 2-Cys peroxiredoxins sensitive to oxidative stress (2010) J Biol Chem., 285, pp. 34485-34492
• Pe'er, I., Felder, C.E., Man, O., Silman, I., Sussman, J.L., Beckmann, J.S., Proteomic signatures: Amino acid and oligopeptide compositions differentiate among phyla (2004) Proteins., 54, pp. 20-40
• Perillo, N.L., Pace, K.E., Seilhamer, J.J., Baum, L.G., Apoptosis of T cells mediated by galectin-1 (1995) Nature., 378, pp. 736-739
• Rabinovich, G.A., Croci, D.O., Regulatory circuits mediated by lectin-glycan interactions in autoimmunity and cancer (2012) Immunity., 36, pp. 322-335
• Rabinovich, G.A., Ilarregui, J.M., Conveying glycan information into T-cell homeostatic programs: A challenging role for galectin-1 in inflammatory and tumor microenvironments (2009) Immunol Rev., 230, pp. 144-159
• Riddles, P.W., Blakeley, R.L., Zerner, B., Ellmans reagent-5,5′-dithiobis (2-nitrobenzoic acid)-Re-examination (1979) Anal Biochem., 94, pp. 75-81
• Shahwan, M., Al-Qirim, M.T., Zaidi, S.M.K.R., Banu, N., Physicochemical properties and amino acid sequence of sheep brain galectin-1 (2004) Biochemistry (Moscow)., 69, pp. 506-512
• Starossom, S.C., Mascanfroni, I.D., Imitola, J., Cao, L., Raddassi, K., Hernandez, S.F., Bassil, R., Delacour, D., Galectin-1 deactivates classically activated microglia and protects from inflammation-induced neurodegeneration (2012) Immunity., 37, pp. 249-263
• Still, W.C., Tempczyrk, A., Hawley, R.C., Hendrickson, T., Semianalytical treatment of solvation for molecular mechanics and dynamics (1990) J Am Chem Soc., 112, pp. 6127-6129
• Stone, J.R., Yang, S., Hydrogen peroxide: A signaling messenger (2006) Antioxid Redox Sign., 8, pp. 243-270
• Stowell, S.R., Cho, M., Feasley, C.L., Arthur, C.M., Song, X., Colucci, J.K., Karmakar, S., McEver, R.P., Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation (2009) J Biol Chem., 284, pp. 4989-4999
• St-Pierre, C., Manya, H., Ouellet, M., Clark, G.F., Endo, T., Tremblay, M.J., Sato, S., Galectin-1-specific inhibitors as a new class of compounds to treat HIV-1 infection (2011) J Virol., 85, pp. 11742-11751
• Than, N.G., Romero, R., Erez, O., Weckle, A., Tarca, A.L., Hotra, J., Abbas, A., Kusanovic, J.P., Emergence of hormonal and redox regulation of galectin-1 in placental mammals: Implication in maternal-fetal immune tolerance (2008) Proc Natl Acad Sci USA., 105, pp. 15819-15824
• Thijssen, V.L., Rabinovich, G.A., Griffioen, A.W., Vascular galectins: Regulators of tumor progression and targets for cancer therapy (2013) Cytokine Growth Factor Rev., 24, pp. 547-558
• Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res., 22, pp. 4673-4680
• Toscano, M.A., Bianco, G.A., Ilarregui, J.M., Croci, D.O., Correale, J., Hernandez, J.D., Zwirner, N.W., Baum, L.G., Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death (2007) Nat Immunol., 8, pp. 825-834
• Tracey, B.M., Feizi, T., Abbott, W.M., Carruthers, R.A., Green, B.N., Lawson, A.M., Subunit molecular mass assignment of 14,654 Da to the soluble beta-galactoside-binding lectin from bovine heart muscle and demonstration of intramolecular disulfide bonding associated with oxidative inactivation (1992) J Biol Chem., 267, pp. 10342-10347
• Trujillo, M., Ferrer-Sueta, G., Thomson, L., Flohé, L., Radi, R., Kinetics of peroxiredoxins and their role in the decomposition of peroxynitrite (2007) Subcell Biochem., 44, pp. 83-113
• Van Gunsteren, W.F., Berendsen, H.J.C., Computer simulation of molecular dynamics: Methodology, applications, and perspectives in chemistry (1990) Angew Chem Int Ed Engl., 29, pp. 992-1023
• Vasta, G.R., Ahmed, H., (2009) Animal Galectins, , Boca Raton, FL CRC Press
• Veal, E., Day, A., Hydrogen peroxide as a signaling molecule (2011) Antioxid Redox Sign., 15, pp. 147-151
• Whitney, P., Powell, J.T., Sanford, G.L., Oxidation and chemical modification of lung beta-galactoside-specific lectin (1986) Biochem J., 238, pp. 683-689
• Winterbourn, C.C., Metodiewa, D., Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide (1999) Free Radic Biol Med., 27, pp. 322-328
• Zou, X., Sun, Y., Kuntz, I.D., Inclusion of solvation in ligand binding free energy calculations using the generalized-Born model (1999) J Am Chem Soc., 121, pp. 8033-8043

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------